Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology.

Abstract	Phosphoinositides play a central role in the control of several cellular events including actin cytoskeleton organization. Here we show that, upon infection of epithelial cells with the Gram-negative pathogen Shigella flexneri, the virulence factor IpgD is translocated directly into eukaryotic cells and acts as a potent inositol 4-phosphatase that specifically dephosphorylates phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P(2)] into phosphatidylinositol 5-monophosphate [PtdIns(5)P] that then accumulates. Transfection experiments indicate that the transformation of PtdIns(4,5)P(2) into PtdIns(5)P by IpgD is responsible for dramatic morphological changes of the host cell, leading to a decrease in membrane tether force associated with membrane blebbing and actin filament remodelling. These data provide the molecular basis for a new mechanism employed by a pathogenic bacterium to promote membrane ruffling at the entry site.
Authors	Kirsten Niebuhr, Sylvie Giuriato, Thierry Pedron, Dana J Philpott, Frédérique Gaits, Julia Sable, Michael P Sheetz, Claude Parsot, Philippe J Sansonetti, Bernard Payrastre
Journal	The EMBO journal (EMBO J) Vol. 21 Issue 19 Pg. 5069-78 (Oct 01 2002) ISSN: 0261-4189 [Print] England
PMID	12356723 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Bacterial Proteins Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates Recombinant Fusion Proteins phosphatidylinositol 5-phosphate Phosphatidylinositol 3-Kinases IpgD protein, Shigella flexneri Phosphoric Monoester Hydrolases
Topics	3T3 Cells Animals Bacterial Proteins (metabolism) Cell Adhesion Enzyme Activation HeLa Cells Humans Kinetics Mice Mutagenesis, Site-Directed Phosphatidylinositol 3-Kinases (metabolism) Phosphatidylinositol 4,5-Diphosphate (metabolism) Phosphatidylinositol Phosphates (metabolism) Phosphoric Monoester Hydrolases (metabolism) Polymerase Chain Reaction Recombinant Fusion Proteins (metabolism) Shigella flexneri (enzymology) Transfection

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